ID T1HU97_RHOPR Unreviewed; 447 AA.
AC T1HU97;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 2.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
DE Flags: Fragment;
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC007617-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC007617-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
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DR EMBL; ACPB03000737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1HU97; -.
DR STRING; 13249.T1HU97; -.
DR EnsemblMetazoa; RPRC007617-RA; RPRC007617-PA; RPRC007617.
DR VEuPathDB; VectorBase:RPRC007617; -.
DR eggNOG; KOG0506; Eukaryota.
DR HOGENOM; CLU_654854_0_0_1; -.
DR InParanoid; T1HU97; -.
DR OrthoDB; 3151390at2759; -.
DR Proteomes; UP000015103; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT REPEAT 372..404
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 447 AA; 50102 MW; 72A69AD9F4B91AFC CRC64;
MVIPKFEELR HAVGVLYGEI EGDVTGETSN YIPEIKNTCP DLWAVSICST DGQKCSFGDY
LVPLTIQDIS YPFLYAKCLD LFGSATVLEY VGIERKPADV SVKNSKANNR AFNPMTDSGA
ISLSTLFCDN DKRTGTAADK HYEFFEFMKA LCGNNHFQIC TPAYVSVRQK DDLSRSIAYA
MLNQGHLPND TDIPTIMDFY FEARSLEVTC DGLAVMAATL ANFGVNPYTN EKLISPISVK
AVLSAMHNWG NYGYSGVNAF YLGLPSKHSV AGAFMVVVPG MLGLILYSPR INDNEVGEKN
IDFAMKFVKK FDLHPLSNSS KEMKKRFGTR KIPEVPCENY CKIFTAVFNN DLEEVMNLTK
GNKKIVFEKD LEGRTILHLA AIKGHFEIIK FVTSNFRKLS SVKDRFGRVP REYVKASDKN
FFEITNIFKK WEDLDKICEL ASASNIN
//